High-resolution iron X-ray absorption spectroscopic and computational studies of non-heme diiron peroxo intermediates.

ABSTRACT: Ferritin-like carboxylate-bridged non-heme diiron enzymes activate O₂ for a variety of difficult reactions throughout nature. These reactions often begin by abstraction of hydrogen from strong CH bonds. The enzymes activate O₂ at their diferrous cofactors to form canonical diferric peroxo intermediates, with a range of possible coordination modes. Herein, we explore the ability of high-energy resolution fluorescence detected X-ray absorption spectroscopy (HERFD XAS) to provide insight into the nature of peroxo level intermediates in non-heme diiron proteins. Freeze quenched (FQ) peroxo intermediates from p-aminobenzoate N-oxygenase (AurF), aldehyde-deformylating oxygenase (ADO), and the β subunit of class Ia ribonucleotide reductase from Escherichia coli (Ecβ) are inv

SUBMITTER: Cutsail GE 

PROVIDER: S-EPMC7012765 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature